UniProtKB/Swiss-Prot P11532: Variant p.Gln2937Arg

Dystrophin
Gene: DMD
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Variant information Variant position:

2937 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B The variants are classified into three categories: LP/P, LB/B and US.

LP/P: likely pathogenic or pathogenic.
LB/B: likely benign or benign.
US: uncertain significance

Residue change:

From Glutamine (Q) to Arginine (R) at position 2937 (Q2937R, p.Gln2937Arg). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:

Change from medium size and polar (Q) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:

Lowest score: -4 (low probability of substitution).
Highest score: 11 (high probability of substitution).

More information can be found on the following page
Other resources:

Links to websites of interest for the variant.

Variant rs1800280 [ dbSNP | Ensembl ]

Sequence information Variant position:

2937 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

3685 The length of the canonical sequence.
Location on the sequence:

KLNLHSADWQRKIDETLERL Q ELQEATDELDLKLRQAEVIK The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         KLNLHSADWQRKIDETLERLQELQEATDELDLKLRQAEVIK

                              KLNVHSADWQRKIDEALERLQELQEATDELDLKLRQAEVIK

Mouse                         KLNLRSADWQRKIDEALERLQELQEAADELDLKLRQAEVIK

Rat                           KLNLHSADWQRKIDEALERLQELQEAADELDLKLRQAEVIK

Pig                           KLNLHSADWQRKIDEALERLQELQEATDELDLKLRQAEVIK

Chicken                       KLNLRSADWQKKIDDALERLQGLQEAMDELDLKLRQAEAFK

Caenorhabditis elegans        ELGIEVESWDKLVQHAMQRLQELERNLAECQLHLTSSENEI

Sequence annotation in neighborhood:

The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:

Type: the type of sequence feature.
Positions: endpoints of the sequence feature.
Description: contains additional information about the feature.

Type	Positions	Description
Chain	1 – 3685	Dystrophin
Repeat	2935 – 3040	Spectrin 24
Alternative sequence	1 – 3068	Missing. In isoform 12, isoform 13, isoform 14, isoform 15, isoform 16 and isoform 17.

Literature citations
The DNA sequence of the human X chromosome.
Ross M.T.; Grafham D.V.; Coffey A.J.; Scherer S.; McLay K.; Muzny D.; Platzer M.; Howell G.R.; Burrows C.; Bird C.P.; Frankish A.; Lovell F.L.; Howe K.L.; Ashurst J.L.; Fulton R.S.; Sudbrak R.; Wen G.; Jones M.C.; Hurles M.E.; Andrews T.D.; Scott C.E.; Searle S.; Ramser J.; Whittaker A.; Deadman R.; Carter N.P.; Hunt S.E.; Chen R.; Cree A.; Gunaratne P.; Havlak P.; Hodgson A.; Metzker M.L.; Richards S.; Scott G.; Steffen D.; Sodergren E.; Wheeler D.A.; Worley K.C.; Ainscough R.; Ambrose K.D.; Ansari-Lari M.A.; Aradhya S.; Ashwell R.I.; Babbage A.K.; Bagguley C.L.; Ballabio A.; Banerjee R.; Barker G.E.; Barlow K.F.; Barrett I.P.; Bates K.N.; Beare D.M.; Beasley H.; Beasley O.; Beck A.; Bethel G.; Blechschmidt K.; Brady N.; Bray-Allen S.; Bridgeman A.M.; Brown A.J.; Brown M.J.; Bonnin D.; Bruford E.A.; Buhay C.; Burch P.; Burford D.; Burgess J.; Burrill W.; Burton J.; Bye J.M.; Carder C.; Carrel L.; Chako J.; Chapman J.C.; Chavez D.; Chen E.; Chen G.; Chen Y.; Chen Z.; Chinault C.; Ciccodicola A.; Clark S.Y.; Clarke G.; Clee C.M.; Clegg S.; Clerc-Blankenburg K.; Clifford K.; Cobley V.; Cole C.G.; Conquer J.S.; Corby N.; Connor R.E.; David R.; Davies J.; Davis C.; Davis J.; Delgado O.; Deshazo D.; Dhami P.; Ding Y.; Dinh H.; Dodsworth S.; Draper H.; Dugan-Rocha S.; Dunham A.; Dunn M.; Durbin K.J.; Dutta I.; Eades T.; Ellwood M.; Emery-Cohen A.; Errington H.; Evans K.L.; Faulkner L.; Francis F.; Frankland J.; Fraser A.E.; Galgoczy P.; Gilbert J.; Gill R.; Gloeckner G.; Gregory S.G.; Gribble S.; Griffiths C.; Grocock R.; Gu Y.; Gwilliam R.; Hamilton C.; Hart E.A.; Hawes A.; Heath P.D.; Heitmann K.; Hennig S.; Hernandez J.; Hinzmann B.; Ho S.; Hoffs M.; Howden P.J.; Huckle E.J.; Hume J.; Hunt P.J.; Hunt A.R.; Isherwood J.; Jacob L.; Johnson D.; Jones S.; de Jong P.J.; Joseph S.S.; Keenan S.; Kelly S.; Kershaw J.K.; Khan Z.; Kioschis P.; Klages S.; Knights A.J.; Kosiura A.; Kovar-Smith C.; Laird G.K.; Langford C.; Lawlor S.; Leversha M.; Lewis L.; Liu W.; Lloyd C.; Lloyd D.M.; Loulseged H.; Loveland J.E.; Lovell J.D.; Lozado R.; Lu J.; Lyne R.; Ma J.; Maheshwari M.; Matthews L.H.; McDowall J.; McLaren S.; McMurray A.; Meidl P.; Meitinger T.; Milne S.; Miner G.; Mistry S.L.; Morgan M.; Morris S.; Mueller I.; Mullikin J.C.; Nguyen N.; Nordsiek G.; Nyakatura G.; O'dell C.N.; Okwuonu G.; Palmer S.; Pandian R.; Parker D.; Parrish J.; Pasternak S.; Patel D.; Pearce A.V.; Pearson D.M.; Pelan S.E.; Perez L.; Porter K.M.; Ramsey Y.; Reichwald K.; Rhodes S.; Ridler K.A.; Schlessinger D.; Schueler M.G.; Sehra H.K.; Shaw-Smith C.; Shen H.; Sheridan E.M.; Shownkeen R.; Skuce C.D.; Smith M.L.; Sotheran E.C.; Steingruber H.E.; Steward C.A.; Storey R.; Swann R.M.; Swarbreck D.; Tabor P.E.; Taudien S.; Taylor T.; Teague B.; Thomas K.; Thorpe A.; Timms K.; Tracey A.; Trevanion S.; Tromans A.C.; d'Urso M.; Verduzco D.; Villasana D.; Waldron L.; Wall M.; Wang Q.; Warren J.; Warry G.L.; Wei X.; West A.; Whitehead S.L.; Whiteley M.N.; Wilkinson J.E.; Willey D.L.; Williams G.; Williams L.; Williamson A.; Williamson H.; Wilming L.; Woodmansey R.L.; Wray P.W.; Yen J.; Zhang J.; Zhou J.; Zoghbi H.; Zorilla S.; Buck D.; Reinhardt R.; Poustka A.; Rosenthal A.; Lehrach H.; Meindl A.; Minx P.J.; Hillier L.W.; Willard H.F.; Wilson R.K.; Waterston R.H.; Rice C.M.; Vaudin M.; Coulson A.; Nelson D.L.; Weinstock G.; Sulston J.E.; Durbin R.M.; Hubbard T.; Gibbs R.A.; Beck S.; Rogers J.; Bentley D.R.;
Nature 434:325-337(2005)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]; VARIANT ARG-2937; Novel small mutations along the DMD/BMD gene associated with different phenotypes.
Nigro V.; Nigro G.; Esposito M.G.; Comi L.I.; Molinari A.M.; Puca G.A.; Politano L.;
Hum. Mol. Genet. 3:1907-1908(1994)
Cited for: VARIANTS HIS-365; TRP-2191 AND ARG-2937; Mutations in the dystrophin gene are associated with sporadic dilated cardiomyopathy.
Feng J.; Yan J.; Buzin C.H.; Towbin J.A.; Sommer S.S.;
Mol. Genet. Metab. 77:119-126(2002)
Cited for: VARIANTS CMD3B ASN-18 AND LEU-3228; VARIANTS TRP-2155; THR-2299; GLN-2366; VAL-2910; ASP-2912 AND ARG-2937;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.